ID A0A2N5SYN3_9BASI Unreviewed; 857 AA.
AC A0A2N5SYN3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA replication licensing factor MCM3 {ECO:0000256|RuleBase:RU368061};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU368061};
GN ORFNames=PCANC_14195 {ECO:0000313|EMBL:PLW18349.1}, PCASD_02825
GN {ECO:0000313|EMBL:PLW48888.1}, PCASD_15898
GN {ECO:0000313|EMBL:PLW22353.1};
OS Puccinia coronata f. sp. avenae.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=200324 {ECO:0000313|EMBL:PLW18349.1, ECO:0000313|Proteomes:UP000235388};
RN [1] {ECO:0000313|Proteomes:UP000235388, ECO:0000313|Proteomes:UP000235392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12NC29 {ECO:0000313|EMBL:PLW18349.1}, and 12SD80
RC {ECO:0000313|EMBL:PLW22353.1};
RA Miller M.E., Zhang Y., Omidvar V., Sperschneider J., Schwessinger B.,
RA Raley C., Palmer J.M., Garnica D., Upadhyaya N., Rathjen J., Taylor J.M.,
RA Park R.F., Dodds P.N., Hirsch C.D., Kianian S.F., Figueroa M.;
RT "De novo assembly and phasing of dikaryotic genomes from two isolates of
RT Puccinia coronata f. sp. avenae, the causal agent of oat crown rust.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which
CC is the replicative helicase essential for 'once per cell cycle' DNA
CC replication initiation and elongation in eukaryotic cells. The active
CC ATPase sites in the MCM2-7 ring are formed through the interaction
CC surfaces of two neighboring subunits such that a critical structure of
CC a conserved arginine finger motif is provided in trans relative to the
CC ATP-binding site of the Walker A box of the adjacent subunit. The six
CC ATPase active sites, however, are likely to contribute differentially
CC to the complex helicase activity. {ECO:0000256|RuleBase:RU368061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU368061};
CC -!- SUBUNIT: Component of the MCM2-7 complex.
CC {ECO:0000256|RuleBase:RU368061}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU368061}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000256|RuleBase:RU004070}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PLW18349.1}.
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DR EMBL; PGCJ01000833; PLW18349.1; -; Genomic_DNA.
DR EMBL; PGCI01000666; PLW22353.1; -; Genomic_DNA.
DR EMBL; PGCI01000020; PLW48888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N5SYN3; -.
DR STRING; 200324.A0A2N5SYN3; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000235388; Unassembled WGS sequence.
DR Proteomes; UP000235392; Unassembled WGS sequence.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IEA:UniProt.
DR GO; GO:0042555; C:MCM complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IEA:UniProt.
DR GO; GO:0043596; C:nuclear replication fork; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032508; P:DNA duplex unwinding; IEA:UniProtKB-UniRule.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0006279; P:premeiotic DNA replication; IEA:UniProt.
DR CDD; cd17754; MCM3; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008046; Mcm3.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF46; DNA REPLICATION LICENSING FACTOR MCM3; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01659; MCMPROTEIN3.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004070};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU368061};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004070};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU368061};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004070};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU368061};
KW Reference proteome {ECO:0000313|Proteomes:UP000235388}.
FT DOMAIN 309..515
FT /note="MCM"
FT /evidence="ECO:0000259|PROSITE:PS50051"
FT REGION 170..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..721
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 94724 MW; 4D19B40915E85756 CRC64;
MDDNQAPAAT YDLPPADPTS NLKDIARIFT EFLDDETRKP NYRILVRKMV EKGERRLIVN
LDDLRDYNRE YCDRLLKTPI EHMAAFELAL SEMVASMAPA DAQTHRRHYV GLRGSFGDHH
VNPRTLRSHM IGKIVSLEGI VTRCSLVRPK VIKSVHFCQE TNQFYEREYR DQLSSGTGPT
STALYPKEDA DGNPLETEFG LSTYMDHQTV AIQEMPERAP AGQLPRSVEV VMDDDLVDNC
KPGDRVQLVG MYRSLGAKGA GGGSATFKTL LVANNVVLLS SKAGGGIAQV QLTELDLRNI
KKVAKRRGVI KLLAESLAPS IFGHEHIKKA VLLMLLGGLE KNLTNGTHIR GDINMLMVGD
PSTAKSQILR FVLNTAPLAI ATTGRGSSGV GLTAAVTTDQ ETGERRLEAG AMVLADRGVV
CIDEFDKMSD VDRVAIHEVM EQQTVTIAKA GIHTSLNARC SVIAAANPIY GQYDVHKDPH
RNIALPDSLL SRFDLLFIVT DDSDEHRDRK ISEHVLRMHR YLQPGVEEGT PAVDVLQQNL
SVGIGIDTMD PGAAKETTVF EKFNPLLHAG LTDTNETRGD SRRKEVLSIE FIKKYIQYAK
NNCKPALTQD AANLIVEVYS SLRNDDLQSN QKKTTPLTAR TLETLIRLAT AHAKARLSPT
VSVADAHGAE AILRFALFKE VMKSRKSQSG HKRRKVDKAK KGVDSDEEEM EDEEESDEGA
NIEETQPVGK SKYPTRSRGA PEATTSGSQP ANQNPSDQME MDPPSIARPI TEESQITGSN
STSSAALTPE RIRLFKQRLG ETFMRSEDSM IEIDELLKLV NEGVQVRLFD EIEAIKILEI
MNEANELMYS SGSIFKI
//
